Editors’ Series: Applications of Native MS and High Resolution Mass Spectrometry for the Characterization of Biotherapeutic Molecules

This presentation will begin on January 29, 2015 at 11:00 AM EST.


Native mass spectrometry preserves the structural integrity of a biomolecule, and can provide valuable information associated with a protein’s multi-meric state, stoichiometry of complexes, and non-covalent interactions with other proteins or small molecules. The less complex spectra typically generated with native MS, such as narrow charge distributions and relatively few charge states, permit a convenient visualization of the various species that are present in the sample mixture. We utilize the excellent resolving power of an orbital ion trap mass spectrometer to interrogate biomolecular complexes and other pharmacological moieties through traditional intact molecular mass determinations under partially denaturing conditions paired with native mass spectrometry. This combination of analyses has facilitated process improvements for a plethora of antibody engineering exercises including single cell co-expression of bispecific antibody products by the low level detection of mispaired species. Native mass spectrometry also has been utilized for visualizing non-covalent higher molecular weight half antibody combinations and for observing antigen binding to bispecifics to infer quantities of doubly mispaired species that would otherwise be unresolvable by molecular mass. Finally, we show the qualitative analysis of binding affinities of small molecule inhibitors to their target enzymes.

To reduce the turnaround time and overall exploration cost, the laboratories have adapted traditional research methods so as to provide meaningful data more rapidly without compromising quality.


Wendy Sandoval
Group Leader, Applied Proteomics

Laura Bush
Editorial Director
LCGC and Spectroscopy

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